Abstract
Thermophilic lactate dehydrogenase (LDH) from Thermotoga maritima demonstrates a drastic increase in Km with increased temperature, compared with that of mesophilic LDH. To investigate such difference and the temperature adaptation of proteins, FTIR is used to probe the structure dependence on the temperature by monitoring amide-I band and CO stretch of oxamate in the ternary complex. It has been found that, although protein denaturing are not observed with an increased temperature up to 80 C (the temperature for optimum growth of Th. maritima), the protein structure as reported by T. Dams et al., shows difference between room temperature and 80 C. FRET and laser induced temperature jump techniques are employed to study the dynamics of ligand-protein complexes of TmLDH on the nanosecond time scale.
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